Evidence map›Paper›PMID 25849926›Full record

ReviewBiochemical Society transactions2015

Chemical reporters for exploring protein acylation.

Emmanuelle Thinon, Howard C Hang

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. ProteinOpen biology · 2021
    Review
  11. A Molecular Perspective on Sirtuin Activity.International journal of molecular sciences · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Greasing the Wheels of Lipid Biology with Chemical Tools.Trends in biochemical sciences · 2018
    Review
  17. Article
  18. Article
  19. Protein S-palmitoylation in cellular differentiation.Biochemical Society transactions · 2017
    Review
  20. Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins.Chembiochem : a European journal of chemical biology · 2016
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Emmanuelle Thinon*Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, U.S.A.
Howard C Hang*Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, U.S.A.
Rockefeller University · US

Funding

Studies on Protein LipidationR01GM087544 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HANG, HOWARD C · 2010 to 2023
$4.4M
NIGMS NIH HHS R01 GM087544NIGMS NIH HHS R01GM087544
6 · The paper itself

Abstract

Proteins are acylated by a variety of metabolites that regulates many important cellular pathways in all kingdoms of life. Acyl groups in cells can vary in structure from the smallest unit, acetate, to modified long-chain fatty acids, all of which can be activated and covalently attached to diverse amino acid side chains and consequently modulate protein function. For example, acetylation of Lys residues can alter the charge state of proteins and generate new recognition elements for protein-protein interactions. Alternatively, long-chain fatty-acylation targets proteins to membranes and enables spatial control of cell signalling. To facilitate the analysis of protein acylation in biology, acyl analogues bearing alkyne or azide tags have been developed that enable fluorescent imaging and proteomic profiling of modified proteins using bioorthogonal ligation methods. Herein, we summarize the currently available acylation chemical reporters and highlight their utility to discover and quantify the roles of protein acylation in biology.

Indexed as

ProteomicsAcylationHumansMetabolic Networks and PathwaysProtein Interaction MapsProtein Processing, Post-TranslationalProteinsProteins

Identifiers

PMID25849926
PMCPMC4529279
OpenAlexW2207047670

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.